TY - JOUR
T1 - How, when and why proteins collapse
T2 - The relation to folding
AU - Haran, Gilad
N1 - NIH [R01GM080515]This work was supported by grant no. R01GM080515 from the NIH. G.H. thanks George Rose for many illuminating discussions, and Inbal Riven for help with graphics and useful comments.
PY - 2012/2
Y1 - 2012/2
N2 - Unfolded proteins under strongly denaturing conditions are highly expanded. However, when the conditions are more close to native, an unfolded protein may collapse to a compact globular structure distinct from the folded state. This transition is akin to the coil-globule transition of homopolymers. Single-molecule FRET experiments have been particularly conducive in revealing the collapsed state under conditions of coexistence with the folded state. The collapse can be even more readily observed in natively unfolded proteins. Time-resolved studies, using FRET and small-angle scattering, have shown that the collapse transition is a very fast event, probably occurring on the submicrosecond time scale. The forces driving collapse are likely to involve both hydrophobic and backbone interactions. The loss of configurational entropy during collapse makes the unfolded state less stable compared to the folded state, thus facilitating folding.
AB - Unfolded proteins under strongly denaturing conditions are highly expanded. However, when the conditions are more close to native, an unfolded protein may collapse to a compact globular structure distinct from the folded state. This transition is akin to the coil-globule transition of homopolymers. Single-molecule FRET experiments have been particularly conducive in revealing the collapsed state under conditions of coexistence with the folded state. The collapse can be even more readily observed in natively unfolded proteins. Time-resolved studies, using FRET and small-angle scattering, have shown that the collapse transition is a very fast event, probably occurring on the submicrosecond time scale. The forces driving collapse are likely to involve both hydrophobic and backbone interactions. The loss of configurational entropy during collapse makes the unfolded state less stable compared to the folded state, thus facilitating folding.
UR - http://www.scopus.com/inward/record.url?scp=84857033993&partnerID=8YFLogxK
U2 - https://doi.org/10.1016/j.sbi.2011.10.005
DO - https://doi.org/10.1016/j.sbi.2011.10.005
M3 - مقالة مرجعية
SN - 0959-440X
VL - 22
SP - 14
EP - 20
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 1
ER -